HSPE1-MOB4 Gene: Structure, Expression, and Clinical Significance | Biomedical Database

HSPE1-MOB4 is a readthrough transcript that spans the adjacent HSPE1 (heat shock protein family E member 1) and MOB4 (MOB family member 4, phocein) genes on chromosome 2. Readthrough transcripts are produced by the splicing of exons from two neighboring genes, resulting in a chimeric mRNA that may encode a fusion protein. The HSPE1-MOB4 readthrough is predicted to produce a protein that combines the chaperonin cofactor domain of HSPE1 with the MOB4/ phocein domain involved in cell cycle and kinase signaling. This gene is listed in the HGNC as a readthrough locus, but its functional significance and protein product have not been fully characterized. The individual genes HSPE1 and MOB4 have well-established roles: HSPE1 encodes a mitochondrial chaperonin cofactor, while MOB4 is involved in cell cycle control and Hippo signaling. The readthrough transcript may represent a regulatory or functional fusion, but evidence is limited.

Tissue Expression

Cell Line Expression

Hotspot Mutations

Mutation functional classification

• Hippo signaling pathway (via MOB4)

• Mitochondrial protein import and folding (via HSPE1)

The HSPE1-MOB4 readthrough transcript is predicted to encode a fusion protein that includes the N-terminal chaperonin cofactor domain from HSPE1 and the C-terminal MOB4/phocein domain. HSPE1 (also known as Hsp10) is a mitochondrial chaperonin that assists in protein folding, while MOB4 is a component of the MOB kinase activator complex involved in cell cycle progression and Hippo signaling. The fusion protein may retain some functions of both domains, but its subcellular localization and activity are unknown. Given the lack of experimental validation, the protein product may not be stably expressed or may be degraded. Further studies are needed to determine if the readthrough protein has physiological relevance.